CLC3_ARATH
ID CLC3_ARATH Reviewed; 258 AA.
AC F4J5M9; O65024;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Clathrin light chain 3;
GN OrderedLocusNames=At3g51890; ORFNames=ATEM1.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10645728; DOI=10.1023/a:1006395324818;
RA Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA Grellet F.;
RT "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT locus on chromosome III.";
RL Plant Mol. Biol. 41:687-700(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles.
CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC chains and 3 light chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic
CC face of coated pits and vesicles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC14416.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF049236; AAC14416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78859.1; -; Genomic_DNA.
DR EMBL; AK228229; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T51160; T51160.
DR RefSeq; NP_566956.4; NM_115048.7.
DR AlphaFoldDB; F4J5M9; -.
DR SMR; F4J5M9; -.
DR IntAct; F4J5M9; 1.
DR STRING; 3702.AT3G51890.1; -.
DR iPTMnet; F4J5M9; -.
DR PaxDb; F4J5M9; -.
DR PRIDE; F4J5M9; -.
DR ProteomicsDB; 246815; -.
DR EnsemblPlants; AT3G51890.1; AT3G51890.1; AT3G51890.
DR GeneID; 824352; -.
DR Gramene; AT3G51890.1; AT3G51890.1; AT3G51890.
DR KEGG; ath:AT3G51890; -.
DR Araport; AT3G51890; -.
DR TAIR; locus:2074378; AT3G51890.
DR eggNOG; ENOG502QVX7; Eukaryota.
DR HOGENOM; CLU_053778_1_0_1; -.
DR InParanoid; F4J5M9; -.
DR OMA; EADKNNW; -.
DR OrthoDB; 1220161at2759; -.
DR PRO; PR:F4J5M9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J5M9; baseline and differential.
DR Genevisible; F4J5M9; AT.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR InterPro; IPR000996; Clathrin_L-chain.
DR PANTHER; PTHR10639; PTHR10639; 1.
DR Pfam; PF01086; Clathrin_lg_ch; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coated pit; Coiled coil; Cytoplasmic vesicle; Membrane;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..258
FT /note="Clathrin light chain 3"
FT /id="PRO_0000413948"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..152
FT /note="Involved in binding clathrin heavy chain"
FT /evidence="ECO:0000250"
FT REGION 224..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..164
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 258 AA; 29183 MW; 566957F373AE2AA0 CRC64;
MSSTLSNEES GLGDSNRSTE VDGGDGGNFT AYESRFQSQR FDSSFSNFDS QPEKESDLPC
GDSSPRPETQ SPPSINSFDD TNDSILPPPS AMEKEEGFAL REWRRLNALR LEEKEKEEKE
MVQQILEAAE QYKAEFYSKR NVTIENNKKL NREKEKFFLE NQEKFYAEAD KNNWKAIAEL
IPREVPVIEN RGNKKKTATI TVIQGPKPGK PTDLSRMRQV LTKLKHNPPT HMKPKLPSPS
GADPNVSVSE QVTVTEKL
